Summary for 3ENL
| Entry DOI | 10.2210/pdb3enl/pdb |
| Descriptor | ENOLASE, SULFATE ION (3 entities in total) |
| Functional Keywords | carbon-oxygen lyase |
| Biological source | Saccharomyces cerevisiae (baker's yeast) |
| Cellular location | Cytoplasm : P00924 |
| Total number of polymer chains | 1 |
| Total formula weight | 46786.75 |
| Authors | Lebioda, L.,Stec, B. (deposition date: 1990-11-13, release date: 1992-04-15, Last modification date: 2024-02-21) |
| Primary citation | Stec, B.,Lebioda, L. Refined structure of yeast apo-enolase at 2.25 A resolution. J.Mol.Biol., 211:235-248, 1990 Cited by PubMed Abstract: The crystal structure of apo-enolase from baker's yeast (Saccharomyces cerevisiae) was established at 2.25 A resolution using a restrained least-squares refinement method. Based on 21,077 independent reflections of better than 8 A resolution, a final R-factor of 15.4% was obtained with a model obeying standard geometry within 0.017 A in bond length and 3.5 degrees in bond angles. The upper limit for the co-ordinate accuracy of the atoms was estimated to be 0.18 A. The refinement confirmed the heterodox, non-parallel character of the 8-fold beta alpha-barrel domain with beta beta alpha alpha(beta alpha)6 topology. The reported structure for which the data were collected at pH 5.0 represents an apo-form of the enzyme. Of the three carboxylic ligands that form the conformational metal ion binding site two, Glu295 and Asp320, are very close and presumably form a strong acidic type hydrogen bond with the proton partially replacing the electric charge of the physiological cofactor Mg2+. The single sulfate ion found in the structure is in the active site cavity, co-ordinated to the side-chains of Lys345 and Arg374, and to the N atom of Ser375. It is located about 7.4 A from the conformational metal ion binding site. It occupies the site in which the phosphate group of the substrate binds. PubMed: 2405163DOI: 10.1016/0022-2836(90)90023-F PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.25 Å) |
Structure validation
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